PDBe 1ito

X-ray diffraction
2.29Å resolution

Crystal Structure Analysis of Bovine Spleen Cathepsin B-E64c complex

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 27.92 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P07688 (Residues: 80-335; Coverage: 81%)
Gene name: CTSB
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 72.578Å b: 72.578Å c: 141.835Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.239